ArticleLife (Basel, Switzerland)2021
A Super Stable Mutant of the Plant Protein Monellin Endowed with Enhanced Sweetness.
Article in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Integrated computation-guided thermostabilization of the fungal sweet protein Honey Truffle Sweetener.Current research in food science · 2026Article
- Boiling-Resistant Single-Chain Sweet Protein Monellin as a Safe and Effective Sugar Alternative for Metabolic and Glycemic Management in Mice.Foods (Basel, Switzerland) · 2025Article
- Beyond Sugar: A Holistic Review of Sweeteners and Their Role in Modern Nutrition.Foods (Basel, Switzerland) · 2025Review
- Expression of a single-chain monellin (MNEI) mutant with enhanced stability in transgenic mice milk.Transgenic research · 2024Article
- Investigating the Effect of Substituting a Single Cysteine Residue on the Thermal Stability of an Engineered Sweet Protein, Single-Chain Monellin.The protein journal · 2023Article
- Brazzein and Monellin: Chemical Analysis, Food Industry Applications, Safety and Quality Control, Nutritional Profile and Health Impacts.Foods (Basel, Switzerland) · 2023Review
- Striking Dependence of Protein Sweetness on Water Quality: The Role of the Ionic Strength.Frontiers in molecular biosciences · 2021Article
- New Insight Into the Structure-Activity Relationship of Sweet-Tasting Proteins: Protein Sector and Its Role for Sweet Properties.Frontiers in nutrition · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sweet proteins are a class of proteins with the ability to elicit a sweet sensation in humans upon interaction with sweet taste receptor T1R2/T1R3. Single-chain Monellin, MNEI, is among the sweetest proteins known and it could replace sugar in many food and beverage recipes. Nonetheless, its use is limited by low stability and high aggregation propensity at neutral pH. To solve this inconvenience, we designed a new construct of MNEI, dubbed Mut9, which led to gains in both sweetness and stability. Mut9 showed an extraordinary stability in acidic and neutral environments, where we observed a melting temperature over 20 °C higher than that of MNEI. In addition, Mut9 resulted twice as sweet than MNEI. Both proteins were extensively characterized by biophysical and sensory analyses. Notably, Mut9 preserved its structure and function even after 10 min boiling, with the greatest differences being observed at pH 6.8, where it remained folded and sweet, whereas MNEI lost its structure and function. Finally, we performed a 6-month shelf-life assessment, and the data confirmed the greater stability of the new construct in a wide range of conditions. These data prove that Mut9 has an even greater potential for food and beverage applications than MNEI.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.